NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 49179 / CS1 / NCTC 12436;
PubMed=9440521 [NCBI, ExPASy, EBI, Israel, Japan]
Bayle D., Waengler S., Weitzenegger T., Steinhilber W., Volz J., Przybylski M., Schaefer K.P., Sachs G., Melchers K.;
"Properties of the P-type ATPases encoded by the copAP operons of Helicobacter pylori and Helicobacter felis.";
J. Bacteriol. 180:317-329(1998).

Comments

FUNCTION: Probably involved in copper export.
CATALYTIC ACTIVITY: ATP + H₂O + Cu²⁺(In) = ADP + phosphate + Cu²⁺(Out).
SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
SIMILARITY: Belongs to the cation transport ATPase (P-type) family. Type IB subfamily.
SIMILARITY: Contains 1 HMA domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AJ001932; CAA05104.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

T47269; T47269.

3D structure databases

HSSP

Q47840; 1CPZ. [HSSP ENTRY / PDB]

ModBase

O32619.

Family and domain databases

InterPro

IPR006416; ATPase-IB_hvy.
IPR001757; ATPase_P.
IPR006403; ATPase_P_cat/Cu.
IPR001756; ATPase_P_Cu.
IPR005834; Dehalogen-like_hydro.
IPR008250; E1-E2_ATPase_reg.
IPR006121; HeavyMe_transpt.
Graphical view of domain structure.

PANTHER

PTHR11939; ATPase_P; 1.

Pfam

PF00122; E1-E2_ATPase; 1.
PF00403; HMA; 1.
PF00702; Hydrolase; 1.
Pfam graphical view of domain structure.

PRINTS

PR00119; CATATPASE.
PR00943; CUATPASE.

TIGRFAMs

TIGR01511; ATPase-IB1_Cu; 1.
TIGR01525; ATPase-IB_hvy; 1.
TIGR01494; ATPase_P-type; 3.

PROSITE

PS00154; ATPASE_E1_E2; 1.
PS01047; HMA_1; 1.
PS50846; HMA_2; 1.
PROSITE graphical view of domain structure (profiles).

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

ATP-binding; Cell membrane; Copper; Copper transport; Hydrolase; Ion transport; Magnesium; Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein; Transmembrane; Transport.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 732`	`732`	`Copper-transporting ATPase.`	`PRO_0000046169`
`TOPO_DOM`	`1 88`	`88`	`Cytoplasmic (Potential).`
`TRANSMEM`	`89 109`	`21`	`Potential.`
`TOPO_DOM`	`110 122`	`13`	`Extracellular (Potential).`
`TRANSMEM`	`123 142`	`20`	`Potential.`
`TOPO_DOM`	`143 149`	`7`	`Cytoplasmic (Potential).`
`TRANSMEM`	`150 170`	`21`	`Potential.`
`TOPO_DOM`	`171 187`	`17`	`Extracellular (Potential).`
`TRANSMEM`	`188 208`	`21`	`Potential.`
`TOPO_DOM`	`209 336`	`128`	`Cytoplasmic (Potential).`
`TRANSMEM`	`337 359`	`23`	`Potential.`
`TOPO_DOM`	`360 365`	`6`	`Extracellular (Potential).`
`TRANSMEM`	`366 383`	`18`	`Potential.`
`TOPO_DOM`	`384 663`	`280`	`Cytoplasmic (Potential).`
`TRANSMEM`	`664 683`	`20`	`Potential.`
`TOPO_DOM`	`684 694`	`11`	`Extracellular (Potential).`
`TRANSMEM`	`695 713`	`19`	`Potential.`
`TOPO_DOM`	`714 732`	`19`	`Cytoplasmic (Potential).`
`DOMAIN`	`3 69`	`67`	`HMA.`
`ACT_SITE`	`421 421`		`4-aspartylphosphate intermediate (By similarity).`
`METAL`	`13 13`		`Copper (Potential).`
`METAL`	`16 16`		`Copper (Potential).`
`METAL`	`609 609`		`Magnesium (By similarity).`
`METAL`	`613 613`		`Magnesium (By similarity).`

Sequence information

Length: 732 AA [This is the length of the unprocessed precursor]

Molecular weight: 78853 Da [This is the MW of the unprocessed precursor]

CRC64: 7105107EA5949EFD [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTKAQFYIEG MTCSACSSGI ERALGRKKFV QEVGVDLISK KAFVVYDENQ ASLEDVFKQI 

        70         80         90        100        110        120 
EKLGYQPRVA TDTPNTFLNP SFLTPNVKLA LVLLGTLGVL ALSMFAPLLP LPSFLKNPFI 

       130        140        150        160        170        180 
NGIVQLVLSL MVMHMGRNFY VHGFKALWAR QPNMDSLIAL GTSAALLYSL VLLFRAYTHA 

       190        200        210        220        230        240 
PIEGYYFESV CVILLFVMAG KRVEENSKDK ALEAMQSLMR HQSLNALKIE NGQSVEVPLE 

       250        260        270        280        290        300 
SLQKGDILQI LPGSYIPVDG VLFKGEAEVD ESMLSGESLP VYKKEGMDLF AGTLNTTTTF 

       310        320        330        340        350        360 
QMRATHTKAQ STLAKILTLI AKAQGSKAPI ARLADKVAGV FVPIVIGIAS IAFLVWLVLG 

       370        380        390        400        410        420 
DFTRALEVFI AILVISCPCA LGLATPMALL VAQKEASLLG LFFKDAVSLE KAKNVNHVIF 

       430        440        450        460        470        480 
DKTGTLTLGT PLVQEVRVAE GVDRLELLTL CASLEAQSEH VIAKGIVAHA KEQGIALQEV 

       490        500        510        520        530        540 
QEVQAKPGFG IKGVVGDQII KAGNLEFFNL PNPFGTLEGI QVFVGTETQI LGVVVLADSL 

       550        560        570        580        590        600 
KEGSKEAISE LKALGVKTTL LSGDNLENVR ALATQLGIQD YHAQAKPEDK LKVIQELKAQ 

       610        620        630        640        650        660 
GKVVMMVGDG VNDAPSLALS DVGVVMAKGS DASLEVADVV SFNNDIQSVV SAMKLSALTI 

       670        680        690        700        710        720 
ANIKQNLFWA FCYNSIAIPL ACGVAYKLGI MFNPMLASLA MSLSSVSVVL NAQRLRGAHF 

       730 
KIRGSHENRH SS

O32619 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools